Detail Information for IndEnz0002002254
IED ID IndEnz0002002254
Enzyme Type ID protease002254
Protein Name Lipoprotein signal peptidase
EC 3.4.23.36
Prolipoprotein signal peptidase
Signal peptidase II
SPase II
Gene Name lspA CTLon_0661
Organism Chlamydia trachomatis serovar L2b (strain UCH-1/proctitis)
Taxonomic Lineage cellular organisms Bacteria PVC group Chlamydiae Chlamydiia Chlamydiales Chlamydiaceae Chlamydia/Chlamydophila group Chlamydia Chlamydia trachomatis Chlamydia trachomatis serovar L2b (strain UCH-1/proctitis)
Enzyme Sequence MPTRSLPTFLTLLLLASIDWVSKLVVLLKSCQLSPHSSAFLYSYVWGHFSFLIIPSFNEGAAFGLFAQYKIPLLIFRVCVILGLALFLRIKYKSLHRRTRIALTLILAGALGNVGDILLHGKVVDFLFLSYYSWRFPSFNLADAFISIGTLLLIGHLYFNKESKKCF
Enzyme Length 167
Uniprot Accession Number B0BC43
Absorption
Active Site ACT_SITE 125; /evidence=ECO:0000255|HAMAP-Rule:MF_00161; ACT_SITE 143; /evidence=ECO:0000255|HAMAP-Rule:MF_00161
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, in which Xaa is hydrophobic (preferably Leu), and Yaa (Ala or Ser) and Zaa (Gly or Ala) have small, neutral side chains.; EC=3.4.23.36; Evidence={ECO:0000255|HAMAP-Rule:MF_00161};
DNA Binding
EC Number 3.4.23.36
Enzyme Function FUNCTION: This protein specifically catalyzes the removal of signal peptides from prolipoproteins. {ECO:0000255|HAMAP-Rule:MF_00161}.
Temperature Dependency
PH Dependency
Pathway PATHWAY: Protein modification; lipoprotein biosynthesis (signal peptide cleavage). {ECO:0000255|HAMAP-Rule:MF_00161}.
nucleotide Binding
Features Active site (2); Chain (1); Transmembrane (5)
Keywords Aspartyl protease;Cell inner membrane;Cell membrane;Hydrolase;Membrane;Protease;Transmembrane;Transmembrane helix
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_00161}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00161}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 18,911
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda